dbPTM

UROK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UROK_HUMAN
UniProt AC	P00749
Protein Name	Urokinase-type plasminogen activator
Gene Name	PLAU
Organism	Homo sapiens (Human).
Sequence Length	431
Subcellular Localization	Secreted.
Protein Description	Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin..
Protein Sequence	MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	CDCLNGGTCVSNKYF CCCCCCCCEECCCCC	15.90	-
38	O-linked_Glycosylation	CDCLNGGTCVSNKYF CCCCCCCCEECCCCC	15.90	2023947
41	Phosphorylation	LNGGTCVSNKYFSNI CCCCCEECCCCCCCC	29.74	-
44	Nitration	GTCVSNKYFSNIHWC CCEECCCCCCCCEEE	19.25	-
158	O-linked_Glycosylation	CADGKKPSSPPEELK CCCCCCCCCCHHHHH	65.44	9765311
158	Phosphorylation	CADGKKPSSPPEELK CCCCCCCCCCHHHHH	65.44	9765311
159	Phosphorylation	ADGKKPSSPPEELKF CCCCCCCCCHHHHHC	53.66	29396449
316	Phosphorylation	FGTSCEITGFGKENS CCCCEEEECCCCCCC	12.26	26074081
322	N-linked_Glycosylation	ITGFGKENSTDYLYP EECCCCCCCCCCCCH	54.41	UniProtKB CARBOHYD
323	Phosphorylation	TGFGKENSTDYLYPE ECCCCCCCCCCCCHH	24.60	2023947
324	Phosphorylation	GFGKENSTDYLYPEQ CCCCCCCCCCCCHHH	40.00	26074081
326	Phosphorylation	GKENSTDYLYPEQLK CCCCCCCCCCHHHHH	14.28	26074081
328	Phosphorylation	ENSTDYLYPEQLKMT CCCCCCCCHHHHHHH	9.86	26074081
335	Phosphorylation	YPEQLKMTVVKLISH CHHHHHHHHHHHHCC	22.14	26074081
341	Phosphorylation	MTVVKLISHRECQQP HHHHHHHCCCCCCCC	27.25	26074081
389	Phosphorylation	CSLQGRMTLTGIVSW EEECCCEEEEEEEEE	21.58	25002506
391	Phosphorylation	LQGRMTLTGIVSWGR ECCCEEEEEEEEECC	18.72	25002506
395	Phosphorylation	MTLTGIVSWGRGCAL EEEEEEEEECCCCCC	23.15	25002506
424	Ubiquitination	PWIRSHTKEENGLAL HHHHHCCCCCCCCCC	58.57	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
158	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
158	S	Phosphorylation	Kinase	PKCA	P05696	PSP
323	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
323	S	Phosphorylation	Kinase	PKCA	P05696	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
158	S	Phosphorylation	9151681
Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding.
323	S	Phosphorylation	9151681
Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of UROK_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAI1_HUMAN	SERPINE1	physical	9184208
GDN_HUMAN	SERPINE2	physical	9184208
IPSP_HUMAN	SERPINA5	physical	2752144
PAI2_HUMAN	SERPINB2	physical	8388810
MP2K1_HUMAN	MAP2K1	genetic	10402467
RASH_HUMAN	HRAS	genetic	10402467
UPAR_HUMAN	PLAUR	physical	16879932
PDGFC_HUMAN	PDGFC	physical	22035541
SCAM5_HUMAN	SCAMP5	physical	21163940
ELAV1_HUMAN	ELAVL1	physical	14517288
GDN_HUMAN	SERPINE2	physical	26186194
MOCOS_HUMAN	MOCOS	physical	26186194
PP4R4_HUMAN	PPP4R4	physical	26186194
GDN_HUMAN	SERPINE2	physical	28514442
MOCOS_HUMAN	MOCOS	physical	28514442
KAT8_HUMAN	KAT8	physical	24953651

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601709	Quebec platelet disorder (QPD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UROK_HUMAN

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Characterization of a posttranslational fucosylation in the growthfactor domain of urinary plasminogen activator."; Buko A.M., Kentzer E.J., Petros A., Menon G., Zuiderweg E.R.,Sarin V.K.; Proc. Natl. Acad. Sci. U.S.A. 88:3992-3996(1991). Cited for: PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, AND MASSSPECTROMETRY.	2023947 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of human pro-urokinase on Ser138/303 impairs itsreceptor-dependent ability to promote myelomonocytic adherence andmotility."; Franco P., Iaccarino C., Chiaradonna F., Brandazza A., Iavarone C.,Mastronicola M.R., Nolli M.L., Stoppelli M.P.; J. Cell Biol. 137:779-791(1997). Cited for: PHOSPHORYLATION AT SER-158 AND SER-323, AND MUTAGENESIS OF SER-158 ANDSER-323.	9151681 [Abstract]